Rapid On-Chip Synthesis of Complex Glycomimetics from N-Glycan Scaffolds for Improved Lectin Targeting.
Identifieur interne : 000074 ( Main/Exploration ); précédent : 000073; suivant : 000075Rapid On-Chip Synthesis of Complex Glycomimetics from N-Glycan Scaffolds for Improved Lectin Targeting.
Auteurs : Anna Cioce [Espagne] ; Michel Thépaut [France] ; Franck Fieschi [France] ; Niels-Christian Reichardt [Espagne]Source :
- Chemistry (Weinheim an der Bergstrasse, Germany) [ 1521-3765 ] ; 2020.
Abstract
C-type lectin receptor (CLR) carbohydrate binding proteins found on immune cells with important functions in pathogen recognition as well as self and non-self-differentiation are increasingly moving into the focus of drug developers as targets for the immune therapy of cancer autoimmune diseases and inflammation and to improve the efficacy of vaccines. The development of molecules with increased affinity and selectivity over the natural glycan binders has largely focused on the synthesis of mono and disaccharide mimetics but glycan array binding experiments have shown increased binding selectivity and affinity for selected larger oligosaccharides that are able to engage in additional favorable interactions beyond the primary binding site. Here, a platform for the rapid preparation and screening of N-glycan mimetics on microarrays is presented that turns a panel of complex glycan core structures into structurally diverse glycomimetics by a combination of enzymatic glycosylation with a nonnatural donor and subsequent cycloaddition with a collection of alkynes. All surface-based reactions were monitored by MALDI-TOF MS to assess conversion and purity of spot compositions. Screening the collection of 374 N-glycomimetics against the plant lectin WFA and the 2 human immune lectins MGL ECD and Langerin ECD produced a number of high affinity binders as lead structures for more selective lectin targeting probes.
DOI: 10.1002/chem.202000026
PubMed: 32445493
Affiliations:
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Christian" sort="Reichardt, Niels Christian" uniqKey="Reichardt N" first="Niels-Christian" last="Reichardt">Niels-Christian Reichardt</name><affiliation wicri:level="1"><nlm:affiliation>CIC biomaGUNE, Paseo Miramón 182, 20009, San Sebastian, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>CIC biomaGUNE, Paseo Miramón 182, 20009, San Sebastian</wicri:regionArea><wicri:noRegion>San Sebastian</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>CIBER-BBN, Paseo Miramón 182, 20009, San Sebastian, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>CIBER-BBN, Paseo Miramón 182, 20009, San Sebastian</wicri:regionArea><wicri:noRegion>San Sebastian</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>Basque Research and Technology Alliance (BRTA), Paseo Miramón 182, 20009, San Sebastian, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Basque Research and Technology Alliance (BRTA), Paseo Miramón 182, 20009, San Sebastian</wicri:regionArea><wicri:noRegion>San Sebastian</wicri:noRegion></affiliation></author></analytic><series><title level="j">Chemistry (Weinheim an der Bergstrasse, Germany)</title><idno type="eISSN">1521-3765</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">C-type lectin receptor (CLR) carbohydrate binding proteins found on immune cells with important functions in pathogen recognition as well as self and non-self-differentiation are increasingly moving into the focus of drug developers as targets for the immune therapy of cancer autoimmune diseases and inflammation and to improve the efficacy of vaccines. The development of molecules with increased affinity and selectivity over the natural glycan binders has largely focused on the synthesis of mono and disaccharide mimetics but glycan array binding experiments have shown increased binding selectivity and affinity for selected larger oligosaccharides that are able to engage in additional favorable interactions beyond the primary binding site. Here, a platform for the rapid preparation and screening of N-glycan mimetics on microarrays is presented that turns a panel of complex glycan core structures into structurally diverse glycomimetics by a combination of enzymatic glycosylation with a nonnatural donor and subsequent cycloaddition with a collection of alkynes. All surface-based reactions were monitored by MALDI-TOF MS to assess conversion and purity of spot compositions. Screening the collection of 374 N-glycomimetics against the plant lectin WFA and the 2 human immune lectins MGL ECD and Langerin ECD produced a number of high affinity binders as lead structures for more selective lectin targeting probes.</div></front></TEI><pubmed><MedlineCitation Status="In-Process" Owner="NLM"><PMID Version="1">32445493</PMID><DateRevised><Year>2020</Year><Month>10</Month><Day>07</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1521-3765</ISSN><JournalIssue CitedMedium="Internet"><Volume>26</Volume><Issue>56</Issue><PubDate><Year>2020</Year><Month>Oct</Month><Day>06</Day></PubDate></JournalIssue><Title>Chemistry (Weinheim an der Bergstrasse, Germany)</Title><ISOAbbreviation>Chemistry</ISOAbbreviation></Journal><ArticleTitle>Rapid On-Chip Synthesis of Complex Glycomimetics from N-Glycan Scaffolds for Improved Lectin Targeting.</ArticleTitle><Pagination><MedlinePgn>12809-12817</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1002/chem.202000026</ELocationID><Abstract><AbstractText>C-type lectin receptor (CLR) carbohydrate binding proteins found on immune cells with important functions in pathogen recognition as well as self and non-self-differentiation are increasingly moving into the focus of drug developers as targets for the immune therapy of cancer autoimmune diseases and inflammation and to improve the efficacy of vaccines. The development of molecules with increased affinity and selectivity over the natural glycan binders has largely focused on the synthesis of mono and disaccharide mimetics but glycan array binding experiments have shown increased binding selectivity and affinity for selected larger oligosaccharides that are able to engage in additional favorable interactions beyond the primary binding site. Here, a platform for the rapid preparation and screening of N-glycan mimetics on microarrays is presented that turns a panel of complex glycan core structures into structurally diverse glycomimetics by a combination of enzymatic glycosylation with a nonnatural donor and subsequent cycloaddition with a collection of alkynes. All surface-based reactions were monitored by MALDI-TOF MS to assess conversion and purity of spot compositions. Screening the collection of 374 N-glycomimetics against the plant lectin WFA and the 2 human immune lectins MGL ECD and Langerin ECD produced a number of high affinity binders as lead structures for more selective lectin targeting probes.</AbstractText><CopyrightInformation>© 2020 Wiley-VCH GmbH.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Cioce</LastName><ForeName>Anna</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>CIC biomaGUNE, Paseo Miramón 182, 20009, San Sebastian, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Thépaut</LastName><ForeName>Michel</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>CNRS, CEA, Institut de Biologie Structurale, Université Grenoble Alpes, 38100, Grenoble, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fieschi</LastName><ForeName>Franck</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>CNRS, CEA, Institut de Biologie Structurale, Université Grenoble Alpes, 38100, Grenoble, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Reichardt</LastName><ForeName>Niels-Christian</ForeName><Initials>NC</Initials><Identifier Source="ORCID">http://orcid.org/0000-0002-9092-7023</Identifier><AffiliationInfo><Affiliation>CIC biomaGUNE, Paseo Miramón 182, 20009, San Sebastian, Spain.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>CIBER-BBN, Paseo Miramón 182, 20009, San Sebastian, Spain.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Basque Research and Technology Alliance (BRTA), Paseo Miramón 182, 20009, San Sebastian, Spain.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>642870</GrantID><Agency>H2020 Marie Skłodowska-Curie Actions</Agency><Country></Country></Grant><Grant><GrantID>CTQ2017-90039-R</GrantID><Agency>Ministerio de Ciencia, Innovación y Universidades</Agency><Country></Country></Grant><Grant><GrantID>RTC-2017-6126-1</GrantID><Agency>Ministerio de Ciencia, Innovación y Universidades</Agency><Country></Country></Grant><Grant><GrantID>MDM-2017-0720</GrantID><Agency>Agencia Estatal de Investigación</Agency><Country></Country></Grant><Grant><GrantID>ANR-15-IDEX-02</GrantID><Agency>Agence Nationale de la Recherche</Agency><Country></Country></Grant><Grant><GrantID>ANR-10-INSB-05-02</GrantID><Agency>Agence Nationale de la Recherche</Agency><Country></Country></Grant><Grant><GrantID>ANR-10- LABX-49-01</GrantID><Agency>Agence Nationale de la Recherche</Agency><Country></Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>09</Month><Day>11</Day></ArticleDate></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Chemistry</MedlineTA><NlmUniqueID>9513783</NlmUniqueID><ISSNLinking>0947-6539</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">glycans</Keyword><Keyword MajorTopicYN="N">glycomimetics</Keyword><Keyword MajorTopicYN="N">lectins</Keyword><Keyword MajorTopicYN="N">microarrays</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2020</Year><Month>01</Month><Day>08</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2020</Year><Month>05</Month><Day>10</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>5</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>5</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>5</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">32445493</ArticleId><ArticleId IdType="doi">10.1002/chem.202000026</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>P. 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HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:32445493" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a PlantImRecepV1
| This area was generated with Dilib version V0.6.38. |  |